ArticleLipids2005
Molecular evidence that the rate-limiting step for the biosynthesis of arachidonic acid in Mortierella alpina is at the level of an elongase.
Article in Lipids, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 44 citations in OpenAlex.
- Novel Approaches toACS omega · 2024Article
- Dietary L-carnitine supplementation changes lipid metabolism and glucose utilization of Rhynchocypris lagowskii fed diets with different lipid sources.Fish physiology and biochemistry · 2024Article
- Construction of DGLA producing cell factory by genetic modification of Mucor circinelloides.Microbial cell factories · 2019Article
- Arachidonic acid production by the oleaginous fungusJournal of advanced research · 2018Review
- Reconstruction and analysis of a genome-scale metabolic model of the oleaginous fungus Mortierella alpina.BMC systems biology · 2015Article
- Article
- Transformation of an oleaginous zygomycete Mortierella alpina 1S-4 with the carboxin resistance gene conferred by mutation of the iron-sulfur subunit of succinate dehydrogenase.Current genetics · 2009Article
- Identification of a sterol Delta7 reductase gene involved in desmosterol biosynthesis in Mortierella alpina 1S-4.Applied and environmental microbiology · 2007Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oil-producing fungus Mortierella alpina 1S-4 is an industrial strain for arachidonic acid (AA) production. To determine its physiological properties and to clarify the biosynthetic pathways for PUFA, heterologous and homologous gene expression systems were established in this fungus. The first trial was performed with an enhanced green fluorescent protein gene to assess the transformation efficiency for heterologous gene expression. As a result, strong fluorescence was observed in the spores of the obtained transformant, suggesting that the foreign gene was inherited by the spores. The next trial was performed with a homologous PUFA elongase (GLELOp) gene, this enzyme having been reported to catalyze the elongation of GLA (18:3n-6) to dihomo-gamma-linolenic acid (20:3n-6), and to be the rate-limiting step of AA production. The FA composition of the transformant was different from that of the host strain: The GLA content was decreased whereas that of AA was increased. These data support the hypothesis that the GLELOp enzyme plays an important role in PUFA synthesis, and may indicate how to control PUFA biosynthesis.
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Registered trials
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